Disease relevance of SLC13A2

• Restriction endonuclease maps were constructed for the genome of a porcine adenovirus (PAV), NADC-1, which was isolated in 1972 from an adult swine [1].
• Using the cloned NADC-1 Bam HI and Eco RI/Bam HI fragments as probes, Southern blot hybridizations were performed to human adenovirus 2 (Ad-2) restriction fragments to determine the left-to-right orientation of the Bam HI and Eco RI/Bam HI fragments [1].
• Several phage-resistant isolates carried a phage that lysed the stock strain of C. fetus subsp. jejuni (NADC 917) [2].
• SDCT (100 mAs effective tube current) and LDCT (20 mAs) of nine patients with pulmonary metastases were obtained within 5 min using four-row detector CT [3].
• The dose-length product (DLP) was estimated for 15 randomly chosen single-detector CT (SDCT) and MDCT adult flank pain examinations using manufacturer's software [4].

High impact information on SLC13A2

• SDCT2, unlike SDCT1, displayed a unique pH dependence for succinate transport (optimal pH 7.5-8.5) and showed a high affinity for dimethylsuccinate, two features characteristic of basolateral transport [5].
• The low affinity Na+/sulfate cotransporter, NaSi-1, belongs to the SLC13 family that also includes the Na+/dicarboxylate cotransporters, NaDC [6].
• The Na+/dicarboxylate cotransporter 1 (NaDC1) is a low-affinity transporter for citric acid cycle intermediates such as succinate and citrate [7].
• The sequence of NaDC1 contains a number of conserved proline residues in predicted transmembrane helices (TMs) 7 and 10 [7].
• Four conserved proline residues in TMs 7 and 10 of rabbit NaDC1 were replaced with alanine to promote ideal alpha helix or glycine to promote free conformation, and the mutant transporters were expressed in the HRPE cell line [7].

Biological context of SLC13A2

• Assignment of the sodium-dependent dicarboxylate transporter gene (SLC13A2 alias NaDC-1) to human chromosome region 17p11.1-->q11.1 by radiation hybrid mapping and fluorescence in situ hybridization [8].
• Substrate specificity of the human renal sodium dicarboxylate cotransporter, hNaDC-3, under voltage-clamp conditions [9].
• The amino acid sequence of hNaDC-1 is 78% identical to the rabbit renal Na(+)-dicarboxylate cotransporter, NaDC-1, and 42% identical to the rat renal Na(+)-sulfate transporter, NaSi-1 [10].
• The gene for hNaDC-1 was localized to chromosome 17 [10].
• Expression of EGFP/SDCT1 fusion protein, subcellular localization signal analysis, tissue distribution and electrophysiological function study [11].

Anatomical context of SLC13A2

• Proximal tubule cells extract dicarboxylates from filtrate and blood, using cotransporters located in the brush border [sodium dicarboxylate cotransporter (NaDC-1)] and basolateral cell membrane (NaDC-3) [9].
• Xenopus oocytes injected with hNaDC-1 cRNA expressed a low-affinity Na(+)-dependent dicarboxylate transporter with Michaelis constant (Km) for succinate around 0.4 mM [10].
• The above-mentioned studies suggest that human SDCT1 protein is located on the lumen membrane of the renal proximal tubule, the C-terminal sequence of the SDCT1 is required for delivery and targeting localization, and the plasma membrane localization signal of the SDCT1 protein maybe locate in the C-terminal sequence [11].
• Recently, the complementary DNAs coding for the Na+/citrate transporters from the apical membranes of rabbit and human kidney, NaDC-1 and hNaDC-1, have been cloned and sequenced [12].
• Expression of the renal Na+/dicarboxylate cotransporter, NaDC-1, in COS-7 cells [13].

Associations of SLC13A2 with chemical compounds

• The transport of succinate by hNaDC-1 was insensitive to the pH of the medium, whereas the transporter of citrate was stimulated by acidic pH [10].
• Two serine residues in hNaSi-1, at positions 260 and 288, are conserved in all of the sulfate transporters in the family whereas the NaDC contain alanine or threonine at those positions [6].
• Then, EGFP-fused wild-type, NH2- and COOH-terminal deletion and point mutants of NaDC3, and chimera between NaDC3 and NaDC1, were generated and transfected into polarized renal cells lines, LLC-PK1 and MDCK [14].
• The other members of the family (NaDC1, NaDC3, and NaCT) are transporters for di- and tri-carboxylates including succinate, citrate and alpha-ketoglutarate [15].
• The unfolding of human apolipoprotein B-100 in its native lipid environment, low density lipoprotein (LDL), and in a soluble, lipid-free complex with sodium deoxycholate (NaDC) has been examined using differential scanning calorimetry (DSC) and near UV circular dichroic (CD) spectroscopy [16].

Other interactions of SLC13A2

• The human Na+-sulfate cotransporter (hNaSi-1) belongs to the SLC13 gene family, which also includes the high-affinity Na+-sulfate cotransporter (hSUT-1) and the Na+-dicarboxylate cotransporters (NaDC) [17].
• Western blot analysis of biotinylated oocyte surface membranes revealed that the co-expression of ClC-5 with ENaC, CFTR, or NaDC-1 decreased the abundance of these proteins at the surface membrane [18].

Analytical, diagnostic and therapeutic context of SLC13A2

• EGFP/SDCT1 mRNAs obtained by in vitro transcription are microinjected into Xenopus laevis oocytes for expression and the trans-membrane currents are measured by using two-microelectrode voltage-clamp technique [11].
• Northern blot analysis indicates that hNaDC-1 mRNA is found in both kidney and intestine [10].
• Using cloned NADC-1 genomic fragments as probes in Southern blot hybridizations, an RE site map was constructed [1].
• Differential scanning calorimetry (DSC) and circular dichroic spectroscopy (CD) were used to investigate the physical properties of apoB in the mixed micellar complex with NaDC and in the vesicular DMPC-apoB complex [19].
• Negative staining experiments were performed in two ways: 1) grids were pulled through NaDC-containing buffer surfaces on which monolayers of apoB had been promoted, or 2) apoB molecules were allowed to diffuse onto carbon surfaces of grids that were floated on sample droplets [20].

References